(data stored in ACNUC7421 zone)

SWISSPROT: LSPA_METNO

ID   LSPA_METNO              Reviewed;         165 AA.
AC   B8IB41;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Lipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE            EC=3.4.23.36 {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Prolipoprotein signal peptidase {ECO:0000255|HAMAP-Rule:MF_00161};
DE   AltName: Full=Signal peptidase II {ECO:0000255|HAMAP-Rule:MF_00161};
DE            Short=SPase II {ECO:0000255|HAMAP-Rule:MF_00161};
GN   Name=lspA {ECO:0000255|HAMAP-Rule:MF_00161};
GN   OrderedLocusNames=Mnod_0392;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein specifically catalyzes the removal of
CC       signal peptides from prolipoproteins. {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   -!- CATALYTIC ACTIVITY: Release of signal peptides from bacterial
CC       membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-
CC       (S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably
CC       Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small,
CC       neutral side chains. {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- PATHWAY: Protein modification; lipoprotein biosynthesis (signal
CC       peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00161}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00161}.
CC   -!- SIMILARITY: Belongs to the peptidase A8 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00161}.
DR   EMBL; CP001349; ACL55434.1; -; Genomic_DNA.
DR   RefSeq; WP_015927145.1; NC_011894.1.
DR   SMR; B8IB41; -.
DR   STRING; 460265.Mnod_0392; -.
DR   MEROPS; A08.001; -.
DR   EnsemblBacteria; ACL55434; ACL55434; Mnod_0392.
DR   KEGG; mno:Mnod_0392; -.
DR   eggNOG; ENOG4105M02; Bacteria.
DR   eggNOG; COG0597; LUCA.
DR   HOGENOM; HOG000096992; -.
DR   KO; K03101; -.
DR   OMA; NRWYFPA; -.
DR   OrthoDB; POG091H059F; -.
DR   UniPathway; UPA00665; -.
DR   Proteomes; UP000008207; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_00161; LspA; 1.
DR   InterPro; IPR001872; Peptidase_A8.
DR   PANTHER; PTHR33695:SF2; PTHR33695:SF2; 1.
DR   Pfam; PF01252; Peptidase_A8; 1.
DR   PRINTS; PR00781; LIPOSIGPTASE.
DR   TIGRFAMs; TIGR00077; lspA; 1.
DR   PROSITE; PS00855; SPASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; B8IB41.
DR   SWISS-2DPAGE; B8IB41.
KW   Aspartyl protease; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    165       Lipoprotein signal peptidase.
FT                                /FTId=PRO_1000123500.
FT   TRANSMEM     64     84       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM     91    111       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   TRANSMEM    127    147       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00161}.
FT   ACT_SITE    109    109       {ECO:0000255|HAMAP-Rule:MF_00161}.
FT   ACT_SITE    136    136       {ECO:0000255|HAMAP-Rule:MF_00161}.
SQ   SEQUENCE   165 AA;  17689 MW;  3BB7EB1BD40F8AB3 CRC64;
     MRPLPFGLLV AAATLVLDQA TKLGLLFLTD LPIRQPIVLA PFAQLVVVWN RGVSYGLFQQ
     HTELGRWLLV AVSVLAAVAL TAWMARTGTR LLAGALGLIV GGAIGNAIDR IAYGAVFDFV
     HLHAGGWSWY VFNVADAGIV LGVAGLLYDA VRAERRNARE IRSDA
//

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